Journal of Industrial Microbiology and Biotechnology

, Volume 31, Issue 11, pp 507–516

Evidence for the existence of PAH-quinone reductase and catechol-O-methyltransferase in Mycobacterium vanbaalenii PYR-1


  • Yong-Hak Kim
    • Division of MicrobiologyNational Center for Toxicological Research
  • Joanna D. Moody
    • Division of MicrobiologyNational Center for Toxicological Research
  • James P. Freeman
    • Division of ChemistryNational Center for Toxicological Research
  • Barbara Brezna
    • Institute of Molecular BiologySlovak Academy of Sciences
  • Karl-Heinrich Engesser
    • Abteilung Biologische Abluftreinigung, ISWAUniversität Stuttgart
    • Division of MicrobiologyNational Center for Toxicological Research
Original Paper

DOI: 10.1007/s10295-004-0178-x

Cite this article as:
Kim, Y., Moody, J.D., Freeman, J.P. et al. J IND MICROBIOL BIOTECHNOL (2004) 31: 507. doi:10.1007/s10295-004-0178-x


Polycyclic aromatic hydrocarbon (PAH) quinone reductase (PQR) and catechol-O-methyltransferase (COMT), from the PAH-degrading Mycobacteriumvanbaalenii PYR-1, were demonstrated to be constitutive enzymes located in the soluble fraction of cell extracts. PQR activities for the reduction of 9,10-phenanthrenequinone and 4,5-pyrene- quinone were 1.40±0.13 and 0.12±0.01 μmol min−1 mg-protein−1, respectively. The exogenous catechols alizarin, anthrarobin, 2,3-dihydroxynaphthalene and esculetin inhibited PQR activity. Anthrarobin (100 μM) and esculetin (100 μM) inhibited 4,5-pyrenequinone reduction by 64–92%. COMT was involved in the O-methylation of 1,2-dihydroxyphenanthrene to form 1-methoxy-2-hydroxyphenanthrene and 1,2-dimethoxyphenanthrene. Both pyrene and 1-hydroxypyrene were metabolized by M. vanbaalenii PYR-1 to form 1-methoxypyrene, 1-methoxy-2-hydroxypyrene, 1-hydroxy-2-methoxypyrene and 1,2-dimethoxypyrene. Among the catechols tested, anthrarobin showed the highest COMT activity (1.06±0.04 nmol/30 min−1 mg-protein−1). These results suggest that the PQR and COMT activities of M. vanbaalenii PYR-1 may play an important role in the detoxification of PAH catechols.


Quinone reductaseCatechol-O-methyltransferasePolycyclic aromatic hydrocarbon

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© Society for Industrial Microbiology 2004